Human RIPK3 maintains MLKL in an inactive conformation prior to cell death by necroptosis

The ancestral origins of the lytic cell death mode, necroptosis, lie in host defense. However, the dysregulation of necroptosis in inflammatory diseases has led to widespread interest in targeting the pathway therapeutically. This mode of cell death is executed by the terminal effector, the MLKL pse...

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Published inNature communications Vol. 12; no. 1; p. 6783
Main Authors Meng, Yanxiang, Davies, Katherine A., Fitzgibbon, Cheree, Young, Samuel N., Garnish, Sarah E., Horne, Christopher R., Luo, Cindy, Garnier, Jean-Marc, Liang, Lung-Yu, Cowan, Angus D., Samson, Andre L., Lessene, Guillaume, Sandow, Jarrod J., Czabotar, Peter E., Murphy, James M.
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 22.11.2021
Nature Publishing Group
Nature Portfolio
Subjects
631/45/275
631/535/1266
631/80/82/2344
82/80
82/83
96
Animals
Apoptosis
Cell death
Cell Death - genetics
Cell Death - physiology
Conformation
Crystal structure
HT29 Cells
Humanities and Social Sciences
Humans
Inflammatory diseases
Kinases
Mice
Mortality
multidisciplinary
Necroptosis
Necroptosis - genetics
Necroptosis - physiology
Phosphorylation
Protein Conformation
Protein Interaction Domains and Motifs
Protein Kinases - chemistry
Protein Kinases - genetics
Protein Kinases - metabolism
Receptor-Interacting Protein Serine-Threonine Kinases - chemistry
Receptor-Interacting Protein Serine-Threonine Kinases - genetics
Receptor-Interacting Protein Serine-Threonine Kinases - metabolism
Recombinant Proteins
Science
Science (multidisciplinary)
Signal Transduction
Upstream
Online AccessGet full text

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Abstract The ancestral origins of the lytic cell death mode, necroptosis, lie in host defense. However, the dysregulation of necroptosis in inflammatory diseases has led to widespread interest in targeting the pathway therapeutically. This mode of cell death is executed by the terminal effector, the MLKL pseudokinase, which is licensed to kill following phosphorylation by its upstream regulator, RIPK3 kinase. The precise molecular details underlying MLKL activation are still emerging and, intriguingly, appear to mechanistically-diverge between species. Here, we report the structure of the human RIPK3 kinase domain alone and in complex with the MLKL pseudokinase. These structures reveal how human RIPK3 structurally differs from its mouse counterpart, and how human RIPK3 maintains MLKL in an inactive conformation prior to induction of necroptosis. Residues within the RIPK3:MLKL C-lobe interface are crucial to complex assembly and necroptotic signaling in human cells, thereby rationalizing the strict species specificity governing RIPK3 activation of MLKL. The pseudokinase MLKL is activated by the upstream kinase RIPK3 in the necroptotic pathway but the structural basis of MLKL activation is not well understood yet. Here, the authors present the crystal structures of the human RIPK3:MLKL complex and human RIPK3 kinase alone, which reveal structural differences between human and murine RIPK3 and they discuss mechanistic implications.
AbstractList The ancestral origins of the lytic cell death mode, necroptosis, lie in host defense. However, the dysregulation of necroptosis in inflammatory diseases has led to widespread interest in targeting the pathway therapeutically. This mode of cell death is executed by the terminal effector, the MLKL pseudokinase, which is licensed to kill following phosphorylation by its upstream regulator, RIPK3 kinase. The precise molecular details underlying MLKL activation are still emerging and, intriguingly, appear to mechanistically-diverge between species. Here, we report the structure of the human RIPK3 kinase domain alone and in complex with the MLKL pseudokinase. These structures reveal how human RIPK3 structurally differs from its mouse counterpart, and how human RIPK3 maintains MLKL in an inactive conformation prior to induction of necroptosis. Residues within the RIPK3:MLKL C-lobe interface are crucial to complex assembly and necroptotic signaling in human cells, thereby rationalizing the strict species specificity governing RIPK3 activation of MLKL.The pseudokinase MLKL is activated by the upstream kinase RIPK3 in the necroptotic pathway but the structural basis of MLKL activation is not well understood yet. Here, the authors present the crystal structures of the human RIPK3:MLKL complex and human RIPK3 kinase alone, which reveal structural differences between human and murine RIPK3 and they discuss mechanistic implications.
The ancestral origins of the lytic cell death mode, necroptosis, lie in host defense. However, the dysregulation of necroptosis in inflammatory diseases has led to widespread interest in targeting the pathway therapeutically. This mode of cell death is executed by the terminal effector, the MLKL pseudokinase, which is licensed to kill following phosphorylation by its upstream regulator, RIPK3 kinase. The precise molecular details underlying MLKL activation are still emerging and, intriguingly, appear to mechanistically-diverge between species. Here, we report the structure of the human RIPK3 kinase domain alone and in complex with the MLKL pseudokinase. These structures reveal how human RIPK3 structurally differs from its mouse counterpart, and how human RIPK3 maintains MLKL in an inactive conformation prior to induction of necroptosis. Residues within the RIPK3:MLKL C-lobe interface are crucial to complex assembly and necroptotic signaling in human cells, thereby rationalizing the strict species specificity governing RIPK3 activation of MLKL.
The ancestral origins of the lytic cell death mode, necroptosis, lie in host defense. However, the dysregulation of necroptosis in inflammatory diseases has led to widespread interest in targeting the pathway therapeutically. This mode of cell death is executed by the terminal effector, the MLKL pseudokinase, which is licensed to kill following phosphorylation by its upstream regulator, RIPK3 kinase. The precise molecular details underlying MLKL activation are still emerging and, intriguingly, appear to mechanistically-diverge between species. Here, we report the structure of the human RIPK3 kinase domain alone and in complex with the MLKL pseudokinase. These structures reveal how human RIPK3 structurally differs from its mouse counterpart, and how human RIPK3 maintains MLKL in an inactive conformation prior to induction of necroptosis. Residues within the RIPK3:MLKL C-lobe interface are crucial to complex assembly and necroptotic signaling in human cells, thereby rationalizing the strict species specificity governing RIPK3 activation of MLKL. The pseudokinase MLKL is activated by the upstream kinase RIPK3 in the necroptotic pathway but the structural basis of MLKL activation is not well understood yet. Here, the authors present the crystal structures of the human RIPK3:MLKL complex and human RIPK3 kinase alone, which reveal structural differences between human and murine RIPK3 and they discuss mechanistic implications.
The pseudokinase MLKL is activated by the upstream kinase RIPK3 in the necroptotic pathway but the structural basis of MLKL activation is not well understood yet. Here, the authors present the crystal structures of the human RIPK3:MLKL complex and human RIPK3 kinase alone, which reveal structural differences between human and murine RIPK3 and they discuss mechanistic implications.
ArticleNumber 6783
Author Luo, Cindy
Fitzgibbon, Cheree
Garnier, Jean-Marc
Garnish, Sarah E.
Liang, Lung-Yu
Sandow, Jarrod J.
Murphy, James M.
Horne, Christopher R.
Czabotar, Peter E.
Davies, Katherine A.
Lessene, Guillaume
Samson, Andre L.
Meng, Yanxiang
Young, Samuel N.
Cowan, Angus D.
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/34811356$$D View this record in MEDLINE/PubMed
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Snippet The ancestral origins of the lytic cell death mode, necroptosis, lie in host defense. However, the dysregulation of necroptosis in inflammatory diseases has...
The pseudokinase MLKL is activated by the upstream kinase RIPK3 in the necroptotic pathway but the structural basis of MLKL activation is not well understood...
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SubjectTerms 631/45/275
631/535/1266
631/80/82/2344
82/80
82/83
96
Animals
Apoptosis
Cell death
Cell Death - genetics
Cell Death - physiology
Conformation
Crystal structure
HT29 Cells
Humanities and Social Sciences
Humans
Inflammatory diseases
Kinases
Mice
Mortality
multidisciplinary
Necroptosis
Necroptosis - genetics
Necroptosis - physiology
Phosphorylation
Protein Conformation
Protein Interaction Domains and Motifs
Protein Kinases - chemistry
Protein Kinases - genetics
Protein Kinases - metabolism
Receptor-Interacting Protein Serine-Threonine Kinases - chemistry
Receptor-Interacting Protein Serine-Threonine Kinases - genetics
Receptor-Interacting Protein Serine-Threonine Kinases - metabolism
Recombinant Proteins
Science
Science (multidisciplinary)
Signal Transduction
Upstream
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Title Human RIPK3 maintains MLKL in an inactive conformation prior to cell death by necroptosis
URI https://link.springer.com/article/10.1038/s41467-021-27032-x
https://www.ncbi.nlm.nih.gov/pubmed/34811356
https://www.proquest.com/docview/2600515780
https://search.proquest.com/docview/2601494439
https://pubmed.ncbi.nlm.nih.gov/PMC8608796
https://doaj.org/article/c906a3851c864c11bf414f6e8e863c7b
Volume 12
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